Crystal Structure of Steroid Reductase SRD5A Reveals Conserved Steroid Reduction Mechanism

    July 2020 in “ bioRxiv (Cold Spring Harbor Laboratory) ”
    Yufei Han, Qian Zhuang, Binyong Sun, Wenping Lv, Sheng Wang, Qi Xiao, Bin Pang, Yiding Zhou, Fuxing Wang, Pengliang Chi, Qisheng Wang, Zhen Li, Lizhe Zhu, Fuping Li, Dong Deng, Ying‐Chih Chiang, Zhenfei Li, Ruobing Ren
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    TLDR The structure of SRD5A reveals how it reduces steroids, aiding drug design for related health conditions.
    The study reported the crystal structure of the steroid 5α-reductase (SRD5A) from Proteobacteria bacterium, revealing a conserved mechanism for NADPH-mediated steroid reduction. The structure, resolved at 2.0 Å, showed that PbSRD5A, which shares significant sequence similarity with human SRD5A1 and SRD5A2, exists as a monomer with seven transmembrane segments. These segments form a hydrophobic cavity for steroid binding and coordinate with NADPH through hydrogen bonds. The findings provided insights into substrate recognition and could aid in designing specific therapeutic molecules targeting SRD5As to treat conditions like benign prostatic hyperplasia, alopecia, prostatic cancer, and infertility.
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